Basic Information | |
---|---|
Species | Ricinus communis |
Cazyme ID | 27698.m000066 |
Family | GT9 |
Protein Properties | Length: 623 Molecular Weight: 68873.7 Isoelectric Point: 7.3578 |
Chromosome | Chromosome/Scaffold: 27698 Start: 644 End: 4787 |
Description | mitochondrial HSO70 2 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GT9 | 90 | 296 | 9.7e-38 |
QAVAAQSYDLVLDLQGLLKSAVMATWARGPRHGYDKHSIREPLASRFYQHQYAIPYRQHAVVRMRTLAAMALGYAVPQNKPAYGLASVGQHAQAAAFLAL HATSRDSKLWPEEYWVALGQHYARQGLHMWLPWASDSEKARAERIAMHVPQALVLPKLGLQQLASQMPQVRFAVGVDTGLSHLAAALDIPIVALYTDTEP ALTGVAG |
Full Sequence |
---|
Protein Sequence Length: 623 Download |
MALYAKIAAM KRILIVKTTS MGDVIHALPV VEDILQHFPD AHIDWLVEES FADIPRLHPR 60 VQRVFTVAVR RWRKQWWRRQ TWREIAVVKQ AVAAQSYDLV LDLQGLLKSA VMATWARGPR 120 HGYDKHSIRE PLASRFYQHQ YAIPYRQHAV VRMRTLAAMA LGYAVPQNKP AYGLASVGQH 180 AQAAAFLALH ATSRDSKLWP EEYWVALGQH YARQGLHMWL PWASDSEKAR AERIAMHVPQ 240 ALVLPKLGLQ QLASQMPQVR FAVGVDTGLS HLAAALDIPI VALYTDTEPA LTGVAGGRVA 300 PAVNLGGKAQ CLRWPRSSRS YQRCAWLRMP KVQEKVKEIF GKEPRKDVNP DEAVAVGAAI 360 QGGVLKGDVK DVLLLDVTPL SLGIETLGSV MTKLIKKNTT IPTKASQVFS TAEDNQNAVT 420 IHVLQGEREM ASGNKSLGQF NLSDIPPSPR GMPQIEVTFD IDANGILHVS AKDKATGKEN 480 KITIKANSGL SEEEIQRMEE DAAKYADEDK KLRELVDARN QADSVLHSVK KSLAEHGDKI 540 EADEKAKIED AIKDLEAVAK DGDDKEVIEA KTNALMEASQ KLGEKVYAEQ QAQANTESAP 600 QAEGEKTVEG DVVDAEFEEV KKD |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
CHL00094 | dnaK | 1.0e-96 | 328 | 619 | 292 | + heat shock protein 70 | ||
TIGR02193 | heptsyl_trn_I | 2.0e-111 | 12 | 312 | 308 | + lipopolysaccharide heptosyltransferase I. This family consists of examples of ADP-heptose:LPS heptosyltransferase I, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]. | ||
pfam00012 | HSP70 | 4.0e-115 | 328 | 588 | 263 | + Hsp70 protein. Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region. | ||
TIGR02350 | prok_dnaK | 9.0e-127 | 328 | 588 | 261 | + chaperone protein DnaK. Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved [Protein fate, Protein folding and stabilization]. | ||
PRK00290 | dnaK | 5.0e-171 | 328 | 623 | 296 | + molecular chaperone DnaK; Provisional |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0005524 | ATP binding |
GO:0008152 | metabolic process |
GO:0016757 | transferase activity, transferring glycosyl groups |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 4b9q_D | 0 | 328 | 591 | 345 | 605 | A Chain A, Open Conformation Of Atp-Bound Hsp70 Homolog Dnak |
PDB | 4b9q_C | 0 | 328 | 591 | 345 | 605 | A Chain A, Open Conformation Of Atp-Bound Hsp70 Homolog Dnak |
PDB | 4b9q_B | 0 | 328 | 591 | 345 | 605 | A Chain A, Open Conformation Of Atp-Bound Hsp70 Homolog Dnak |
PDB | 4b9q_A | 0 | 328 | 591 | 345 | 605 | A Chain A, Open Conformation Of Atp-Bound Hsp70 Homolog Dnak |
PDB | 2kho_A | 0 | 328 | 591 | 345 | 605 | A Chain A, Nmr-Rdc XRAY STRUCTURE OF E. COLI HSP70 (DNAK) CHAPERONE (1-605) Complexed With Adp And Substrate |
Orthologous Group | |||||
---|---|---|---|---|---|
Species | ID | ||||
Picea abies | MA_159042g1050 | MA_159042g1060 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|